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DOI - 10.32743/UniTech.2024.120.3.17029 STUDY OF THE EFFECT OF MODIFIED AMINOALDEHYDE OLIGOMER WITH COLLAGEN
Vohid Akhmedov
Professor
of the Bukhara Institute of Engineering and Technology,
Uzbekistan, Bukhara E-mail: voxid7@mail.ru
Zulfizar Murodova
Researcher
of the Bukhara Institute of Engineering and Technology,
Uzbekistan, Bukhara
Bobir Olimov
Associate Professor of the Bukhara Institute of Engineering and Technology,
Uzbekistan, Bukhara
ИЗУЧЕНИЕ ДЕЙСТВИЯ МОДИФИЦИРОВАННОГО АМИНОАЛЬДЕГИДНОГО ОЛИГОМЕРА С КОЛЛАГЕНОМ
Ахмедов Вохид Низомович
профессор
Бухарского инженерно-технологического института, Республика Узбекистан, г. Бухара
Муродова Зулфизар Олимовна
соискатель
Бухарского инженерно-технологического института, Республика Узбекистан, г. Бухара
Олимов Бобир Баходирович
доцент
Бухарского инженерно-технологического института, Республика Узбекистан, г. Бухара
ABSTRACT
This article provides information on the modification of collagen with modified aminoaldehyde. Information is also given about Van der Waals forces between these molecules. In order to assign different properties to oligomers, knowledge of their molecular properties is required. For this reason, the structure of oligomers and interactions between molecules in them were studied.
АННОТАЦИЯ
В данной статье представлена информация о модификации коллагена модифицированным аминоальдегидом. Также приведены сведения о силах Ван-дер-Ваальса между этими молекулами. Чтобы приписать олигомерам различные свойства, необходимо знание их молекулярных свойств. По этой причине изучались строение олигомеров и взаимодействия между молекулами в них.
Keywords: amide bond, covalent bond, aminoaldehyde oligomers, Wan-der Walls effect, polymer.
Ключевые слова: амидная связь, ковалентная связь, аминоальдегидные олигомеры, эффект Вандера-Валлса, полимер.
Библиографическое описание: Murodova Z., Akhmedov V.N., Olimov B.B. STUDY OF THE EFFECT OF MODIFIED AMINOALDEHYDE OLIGOMER WITH COLLAGEN // Universum: технические науки : электрон. научн. журн. 2024. 3(120). URL: https://7universum. com/ru/tech/archive/item/17029
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Introduction. Today, the demand for aminoaldehyde oligomers in the world is increasing in many other industries, such as wood processing, textiles, production of plastic masses, as well as tanning[1-5]. Its high physico-mechanical, as well as a number of technological, including thermal stability, adhesion properties have led to the further expansion of the areas where aminoaldehyde oligomers are used in recent years. The growing demands for new materials based on aminoaldehyde oligomers and the development of effective methods for studying the effect of the composition and functionality of these compounds on its properties are receiving great attention[6-9].
Materials and methods. When different molecules come close to each other, there is a certain amount of interaction between them. The reason for this effect is the coulomb interaction of the electron and nucleus of one molecule with the electron and nucleus of another molecule[10-14]. Synthesized oligomer binds with free functional groups in leather collagen by forming intermolecular hydrogen (Fig. 1) and chemical bonds (Fig. 2).
Figure 1. Intermolecular and hydrogen bonding formed by collagen oligomers
Figure 2. Mechanism of orientational Van der Waals effect
Results and discussion. Skin collagen with of the oligomer in order to analyze the formation of a mutual bond, it is necessary to have information about its composition and amount. Functional groups in collagen and their amount are shown in Table 1.
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Table 1.
Type and number of functional groups in collagen
Functional groups Meeting 100 g of collagen goods the number
Formula Naming
- COOH carboxylic Asparagine and glutamine acids 0.136
- NH2 a - amino lysine, oxylisine 0.037
h -n- nh2 guanidine Arginine 0.055
-c-n hc ch \/ n h Imide Histidine 0.007
- OH hydroxyl Threonine, oxylisin 0.155
-CO -NH - Amide Amino - and imino acids and integrity 0.955
-c— o - Proline, oxyproline 0.144
Regarding which functional groups of the oligomer functional groups. Table 2 provides information on what
synthesized with the functional groups in Table 1, there type of bond the functional groups form.
should be information about the reactivity of these
Table 2.
It reacts with collagens
Types Connection harvest in being participation collagen groups
Covalent h Acidic (- COOH); basic ( -NH2,) -n-cq nh2 and non-dissociable hydroxyl ( -OH) groups
Electrovalent -nh Acidic (-COO - ) and dissociable reasonable (- NH+ ,-jj-) xnh3+
Hydrogen Peptide groups (- CO - NH-)
Coordination When dissociated acidic ( - COO-)- and not dissociated in the case amino groups ( -NH2)
Based on the data presented in Tables-1, 2 above, we will study the interaction of the oligomer with collagen. Since skin collagen and synthesized oligomer
composition is a polar macromolecule with a dipole moment by its nature, a dipole-dipole effect occurs, and this is an orientational intermolecular (Fig-3.) effect.
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Figure 3. Chemical bonds formed by collagen with oligomers
In this case, the deformation of the electron cloud of the molecule is observed as a result of the effect of the poles. If one of these molecules were non-polar, we would have observed van der Waals induction , but here both molecules are polar. Dispersion Van der Waals effects occur between non-polar molecules, and this effect is not observed in the substances here.
Conclusion. As can be seen from the figure-1, 2, 3, the resulting intermolecular hydrogen bonds migrate due to breaking due to various external influences (due to the low energy of these bonds). However, due to the high
energy of the chemical bond (which is formed between the hydroxyl and amino groups of the synthesized oligomer with the carboxyl of the aspartic acid residue in collagen), external mechanical effects are not enough to break it, and therefore migration is not observed. A clear example of this is the kinetics of degradation during thermal destruction of an oligomer-treated leather sample. It takes a lot of energy to break any chemical bond, which leads to an increase in the service life due to the fact that the leather is not observed during the service life and does not migrate.
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